Myosin di-phosphorylation and peripheral actin bundle formation as initial events during endothelial barrier disruption

Mayumi Hirano, Katsuya Hirano

研究成果: ジャーナルへの寄稿記事

18 引用 (Scopus)

抄録

The phosphorylation of the 20-kD myosin light chain (MLC) and actin filament formation play a key role in endothelial barrier disruption. MLC is either mono- or di-phosphorylated (pMLC and ppMLC) at T18 or S19. The present study investigated whether there are any distinct roles of pMLC and ppMLC in barrier disruption induced by thrombin. Thrombin induced a modest bi-phasic increase in pMLC and a robust mono-phasic increase in ppMLC. pMLC localized in the perinuclear cytoplasm during the initial phase, while ppMLC localized in the cell periphery, where actin bundles were formed. Later, the actin bundles were rearranged into stress fibers, where pMLC co-localized. Rho-kinase inhibitors inhibited thrombin-induced barrier disruption and peripheral localization of ppMLC and actin bundles. The double, but not single, mutation of phosphorylation sites abolished the formation of peripheral actin bundles and the barrier disruption, indicating that mono-phosphorylation of MLC at either T18 or S19 is functionally sufficient for barrier disruption. Namely, the peripheral localization, but not the degree of phosphorylation, is suggested to be essential for the functional effect of ppMLC. These results suggest that MLC phosphorylation and actin bundle formation in cell periphery are initial events during barrier disruption.

元の言語英語
記事番号20989
ジャーナルScientific reports
6
DOI
出版物ステータス出版済み - 2 11 2016

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Myosins
Myosin Light Chains
Actins
Phosphorylation
Thrombin
rho-Associated Kinases
Stress Fibers
Actin Cytoskeleton
Cytoplasm
Mutation

All Science Journal Classification (ASJC) codes

  • General

これを引用

Myosin di-phosphorylation and peripheral actin bundle formation as initial events during endothelial barrier disruption. / Hirano, Mayumi; Hirano, Katsuya.

:: Scientific reports, 巻 6, 20989, 11.02.2016.

研究成果: ジャーナルへの寄稿記事

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